Central and Peripheral Metabolic Defects Contribute to the Pathogenesis of Alzheimer's Disease: Targeting Mitochondria for Diagnosis and Prevention
Open accessAbstract
Significance: Epidemiological studies indicate that metabolic disorders are associated with an increased risk for Alzheimer's disease (AD). Metabolic remodeling occurs in the central nervous system (CNS) and periphery, even in the early stages of AD. Mitochondrial dysfunction has been widely accepted as a molecular mechanism underlying metabolic disorders. Therefore, focusing on early metabolic changes, especially from the perspective of mitochondria, could be of interest for early AD diagnosis and intervention. Recent Advances: We and others have identified that the levels of several metabolites are fluctuated in the periphery before their accumulation in the CNS, which plays an important role in the pathogenesis of AD. Mitochondrial remodeling is likely one of the earliest signs of AD, linking nutritional imbalance to cognitive deficits. Notably, by improving mitochondrial function, mitochondrial nutrients efficiently rescue cellular metabolic dysfunction in the CNS and periphery in individuals with AD. Critical Issues: Peripheral metabolic disorders should be intensively explored and evaluated for the early diagnosis of AD. The circulating metabolites derived from mitochondrial remodeling represent novel potential diagnostic biomarkers for AD that are more readily detected than CNS-oriented biomarkers. Moreover, mitochondrial nutrients provide a promising approach to preventing and delaying AD progression. Future Directions: Abnormal mitochondrial metabolism in the CNS and periphery is involved in AD pathogenesis. More clinical studies provide evidence for the suitability and reliability of circulating metabolites and cytokines for the early diagnosis of AD. Targeting mitochondria to rewire cellular metabolism is a promising approach to preventing AD and ameliorating AD-related metabolic disorders.
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Mitochondrial depolarization was observed in neurons subjected to oligomeric Aβ1-42 direct exposure.
“mitochondrial depolarization was observed in neurons subjected to oligomeric Aβ1–42 direct exposure [63].”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [63]
The “Ab and mitochondria” section says Aβ can decrease mitochondrial membrane potential, supporting the depolarization mechanism. It does not specify an observation in neurons directly exposed to oligomeric Aβ1–42; the separate report of reduced membrane potential concerns transgenic APP mouse brains, not that exposure condition. Page numbers are unavailable in our copy. (LLM, conf=0.84)
Experimental — accuracy not yet measuredNeuropathological features due to Aβ accumulation are related with decrease in respiratory capacity and ATP production, and changes in mitochondrial morphology.
“neuropathological features due to Aβ accumulation have also been related with a decrease in respiratory capacity and ATP production, and changes in mitochondrial morphology [63]”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [63]
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NIA‐AA Research Framework: Toward a biological definition of Alzheimer's disease
Jack, C. R., Bennett, D. A., Blennow, K., Carrillo, M. C., Dunn, B., Haeberlein, S. B., Holtzman, D. M., Jagust, W., Jessen, F., Karlawish, J., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.02.018 · Cited by 10,537 · see citing works
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works
The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · see citing works
Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326 · see citing works
NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898 · see citing works
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441 · see citing works
One-Carbon Metabolism in Health and Disease
Ducker, G. S., & Rabinowitz, J. D. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.009 · Cited by 2,239 · see citing works
Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease
Corder, E. H., Saunders, A. M., Risch, N. J., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Rimmler, J. B., Locke, P. A., Conneally, P. M., Schmader, K. E., et al. (1994) · Nature Genetics · doi:10.1038/ng0694-180 · Cited by 1,920 · see citing works
2018 Alzheimer's disease facts and figures
Alzheimer's Association (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.02.001 · Cited by 1,912 · see citing works
Mitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803 · cited 1× · see citing works
“Oxidative stress arises from excess ROS, most of which are generated from mitochondria by electron leakage from the OXPHOS and TCA cycle and are also generated from pathological AD conditions (110, 404, 420).”
BackgroundLandscape of genetic lesions in 944 patients with myelodysplastic syndromes
Haferlach, T., Nagata, Y., Grossmann, V, Okuno, Y., Bacher, U., Nagae, G., Schnittger, S., Sanada, M., Kon, A., Alpermann, T., et al. (2014) · Leukemia · doi:10.1038/leu.2013.336 · Cited by 1,532 · see citing works
Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513 · see citing works
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224 · see citing works
Alzheimer’s disease: Clinical trials and drug development
Mangialasche, F., Solomon, A., Winblad, B., Mecocci, P., & Kivipelto, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70119-8 · Cited by 1,217 · see citing works
Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., et al. (2012) · Genes & Development · doi:10.1101/gad.191056.112 · Cited by 1,188 · see citing works
Tau-targeting therapies for Alzheimer disease
Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113 · cited 3× · see citing works
“Activating GSK3b, a Tau phosphorylation kinase, could also induce inflammation via NF-jB and lead to apoptosis (62, 277).”
BackgroundExercise and brain neurotrophins
Neeper, S. A., Góauctemez-Pinilla, F., Choi, J., & Cotman, C. (1995) · Nature · doi:10.1038/373109a0 · Cited by 1,066 · see citing works
Trial of Solanezumab for Mild Dementia Due to Alzheimer’s Disease
Honig, L. S., Vellas, B., Woodward, M., Boada, M., Bullock, R., Borrie, M., Hager, K., Andreasen, N., Scarpini, E., Liu-Seifert, H., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1705971 · Cited by 1,049 · cited 1× · see citing works
“Although preclinic and clinical studies show that Ab pathology is the major characteristic of AD, many clinical trials focusing on clearing Ab and decreasing Ab production have failed (8, 162, 209, 234, 405), indicating that track-Abonly is insufficient for AD treatment and that additional mechanisms are essential for…”
BackgroundAugustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998 · see citing works
Ketone bodies as signaling metabolites
Newman, J. C., & Verdin, E. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.002 · Cited by 966 · see citing works
Mitochondria and Mitochondrial Cascades in Alzheimer’s disease
Swerdlow, R. H. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170585 · Cited by 850 · see citing works
Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792 · see citing works
The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.010 · Cited by 786 · see citing works
O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775 · see citing works
GLUT1 reductions exacerbate Alzheimer's disease vasculo-neuronal dysfunction and degeneration
Winkler, E. A., Nishida, Y., Sagare, A. P., Rege, S. V., Bell, R. D., Perlmutter, D., Sengillo, J. D., Hillman, S., Kong, P., Nelson, A. R., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.3966 · Cited by 689 · see citing works
Transcriptional regulation of hepatic lipogenesis
Wang, Y., Viscarra, J., Kim, S.-J., & Sul, H. S. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4074 · Cited by 646 · see citing works
Halagappa, V. K. M., Guo, Z., Pearson, M., Matsuoka, Y., Cutler, R. G., LaFerla, F. M., & Mattson, M. P. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.12.019 · Cited by 580 · see citing works
Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207030 · Cited by 571 · see citing works
The microtubule binding domain of tau protein
Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500 · see citing works
D-β-Hydroxybutyrate rescues mitochondrial respiration and mitigates features of Parkinson disease
Tieu, K., Perier, C., Caspersen, C., Teismann, P., Wu, D.-C., Yan, S.-D., Naini, A., Vila, M., Jackson-Lewis, V., Ramasamy, R., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318797 · Cited by 497 · see citing works
The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production
Pastorino, L., Sun, A., Lu, P.-J., Zhou, X. Z., Balastik, M., Finn, G., Wulf, G., Lim, J., Li, S.-H., Li, X., et al. (2006) · Nature · doi:10.1038/nature04543 · Cited by 487 · see citing works
McManus, M. J., Murphy, M. P., & Franklin, J. L. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0552-11.2011 · Cited by 432 · see citing works
Neuroprotective strategies involving ROS in Alzheimer disease
Dumont, M., & Beal, M. F. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.026 · Cited by 402 · see citing works
Herzig, M. C., Winkler, D. T., Burgermeister, P., Pfeifer, M., Kohler, E., Schmidt, S. D., Danner, S., Abramowski, D., Stürchler-Pierrat, C., Bürki, K., et al. (2004) · Nature Neuroscience · doi:10.1038/nn1302 · Cited by 391 · see citing works
Galasko, D. R., Peskind, E., Clark, C. M., Quinn, J. F., Ringman, J. M., Jicha, G. A., Cotman, C., Cottrell, B., Montine, T. J., Thomas, R. G., et al. (2012) · Archives of Neurology · doi:10.1001/archneurol.2012.85 · Cited by 377 · see citing works
Proteolytic Degradation of Amyloid -Protein
Saido, T., & Leissring, M. A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006379 · Cited by 368 · see citing works
Cardiorespiratory fitness and brain atrophy in early Alzheimer disease.
Burns, J. M., Cronk, B. B., Anderson, H. S., Donnelly, J. E., Thomas, G. P., Harsha, A., Brooks, W. M., & Swerdlow, R. H. (2008) · Neurology · doi:10.1212/01.wnl.0000317094.86209.cb · Cited by 363 · see citing works
Abnormalities of mitochondrial enzymes in Alzheimer disease
Gibson, G. E., Sheu, K.-F. R., & Blass, J. P. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050099 · Cited by 345 · see citing works
Chang, S., Ma, T. R., Miranda, R. D., Balestra, M. E., Mahley, R. W., & Huang, Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508254102 · Cited by 319 · see citing works
Mitochondrial alterations in Alzheimer's disease
Baloyannis, S. J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9204 · Cited by 318 · cited 1× · see citing works
“In early research, several groups observed different types of mitochondrial abnormalities in the brains or peripheral tissues of patients with AD and animal models (22, 157, 248, 270, 354, 419).”
BackgroundApolipoprotein E4 Impairs Neuronal Insulin Signaling by Trapping Insulin Receptor in the Endosomes
Zhao, N., Liu, C.-C., Van Ingelgom, A. J., Martens, Y. A., Linares, C., Knight, J. A., Painter, M. M., Sullivan, P. M., & Bu, G. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.003 · Cited by 289 · cited 1× · see citing works
“Possible mechanisms by which ApoE4 elicits insulin resistance include mediating cerebral blood volume and postprandial responses (185), trapping IR in the endosomes (468), and altering DNA hydroxymethylation and metabolic pathways of purine metabolism, glutamate metabolism, and the pentose phosphate pathway (184).”
BackgroundShinto, L., Quinn, J., Montine, T., Dodge, H. H., Woodward, W., Baldauf-Wagner, S., Waichunas, D., Bumgarner, L., Bourdette, D., Silbert, L., et al. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-130722 · Cited by 288 · see citing works
Durairajan, S. S. K., Liu, L.-F., Lu, J.-H., Chen, L.-L., Yuan, Q., Chung, S. K., Huang, L., Li, X.-S., Huang, J.-D., & Li, M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.016 · Cited by 271 · see citing works
Self-citationBaek, S. H., Park, S. J., Jeong, J. I., Kim, S. H., Han, J., Kyung, J. W., Baik, S.-H., Choi, Y., Choi, B. Y., Park, J. S., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2385-16.2017 · Cited by 258 · see citing works
Dysregulation of lipids in Alzheimer’s disease and their role as potential biomarkers
Wong, M. W., Braidy, N., Poljak, A., Pickford, R., Thambisetty, M., & Sachdev, P. S. (2017) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2017.01.008 · Cited by 223 · see citing works
Low cerebrospinal fluid concentration of mitochondrial DNA in preclinical Alzheimer disease
Podlesniy, P., Figueiro‐Silva, J., Llado, A., Antonell, A., Sanchez‐Valle, R., Alcolea, D., Lleo, A., Molinuevo, J. L., Serra, N., & Trullas, R. (2013) · Annals of Neurology · doi:10.1002/ana.23955 · Cited by 219 · see citing works
Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., & Hisanaga, S.-I. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5927-11.2012 · Cited by 206 · see citing works
Blanch, M., Mosquera, J. L., Ansoleaga, B., Ferrer, I., & Barrachina, M. (2016) · The American Journal of Pathology · doi:10.1016/j.ajpath.2015.10.004 · Cited by 192 · see citing works
Lipids in Alzheimer’s disease: A century-old story
Foley, P. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.05.004 · Cited by 186 · see citing works
Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model
Xie, H., Guan, J., Borrelli, L. A., Xu, J., Serrano-Pozo, A., & Bacskai, B. J. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1836-13.2013 · Cited by 185 · cited 1× · see citing works
“Decreases in respiratory capacity, increases in mitochondrial fragmentation, and fractures in the mitochondrial cristae structure occurs in the AD brain, and the abnormalities in mitochondria appear before pathological Ab plaque deposition (371, 438).”
BackgroundSmith, G. S. (1992) · Archives of Neurology · doi:10.1001/archneur.1992.00530350056020 · Cited by 178 · see citing works
Apolipoprotein E4 Alters Astrocyte Fatty Acid Metabolism and Lipid Droplet Formation
Farmer, B., Kluemper, J., & Johnson, L. (2019) · Cells · doi:10.3390/cells8020182 · Cited by 164 · see citing works
Hastings, N. B., Wang, X., Song, L., Butts, B. D., Grotz, D., Hargreaves, R., Fred Hess, J., Hong, K.-L. K., Huang, C. R.-R., Hyde, L., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0181-0 · Cited by 164 · see citing works
Impaired platelet mitochondrial activity in Alzheimer's disease and mild cognitive impairment
Valla, J., Schneider, L., Niedzielko, T., Coon, K. D., Caselli, R., Sabbagh, M. N., Ahern, G. L., Baxter, L., Alexander, G., Walker, D. G., et al. (2006) · Mitochondrion · doi:10.1016/j.mito.2006.10.004 · Cited by 159 · see citing works
Kumar-Singh, S. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.18.2589 · Cited by 158 · see citing works
Liu, J., Peng, Y., Wang, X., Fan, Y., Qin, C., Shi, L., Tang, Y., Cao, K., Li, H., Long, J., et al. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5b00516 · Cited by 133 · see citing works
Self-citationYoung, M. L., & Franklin, J. L. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103409 · Cited by 120 · see citing works
Sala Frigerio, C., Lau, P., Troakes, C., Deramecourt, V., Gele, P., Van Loo, P., Voet, T., & De Strooper, B. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2015.02.007 · Cited by 71 · see citing works
Pinho, T. S., Correia, S. C., Perry, G., Ambrósio, A. F., & Moreira, P. I. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.037 · Cited by 70 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- Canevelli M, Piscopo P, Talarico G, Vanacore N, Blasimme A, Crestini A, Tosto G, Troili F, Lenzi GL, and Confaloni A. Familial Alzheimer's disease sustained by presenilin 2 mutations: systematic review of literature and genotype-phenotype correlation. Neurosci Biobehav Rev 42: 170-179, 2014.
- Corder EH, Saunders AM, Strittmatter WJ, Schmechel DE, Gaskell PC, Small GW, Roses AD, Haines JL, and Pericak-Vance MA. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261: 921-923, 1993.
Cited by
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Defective mitophagy in Alzheimer’s disease
Pradeepkiran, J. A., & Reddy, P. H. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101191 · Cited by 367 · see citing works
Brain lipidomics: From functional landscape to clinical significance
Yoon, J. H., Seo, Y., Jo, Y. S., Lee, S., Cho, E., Cazenave-Gassiot, A., Shin, Y.-S., Moon, M. H., An, H. J., Wenk, M. R., et al. (2022) · Science Advances · doi:10.1126/sciadv.adc9317 · Cited by 324 · see citing works
Pires, M., & Rego, A. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010778 · Cited by 157 · see citing works
Identification of metabolism-related subtypes and feature genes in Alzheimer’s disease
Lian, P., Cai, X., Wang, C., Liu, K., Yang, X., Wu, Y., Zhang, Z., Ma, Z., Cao, X., & Xu, Y. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04324-y · Cited by 29 · see citing works
- Authors
- Peng, Y., Gao, P., Shi, L., Chen, L., Liu, J., & Long, J.
- Affiliations
- Xi'an Jiaotong University (CN)
- Corresponding author
- Liu, Jiankang
- Long, Jiangang
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2020-04-28
- Volume
- 32
- Issue
- 16
- Pages
- 1188-1236
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC7196371
- OpenAlex
- W3006102624
- Cited by
- 110
- References
- 60
- Citations by year
- 2026: 11 · 2025: 20 · 2024: 22 · 2023: 21 · 2022: 17 · 2021: 11 · 2020: 8
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Antioxidants and Redox Signaling (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (31870848, 31570777, 2015CB856302, 31770917, 81802787, 81741110)
- China Postdoctoral Science Foundation (2018M643673)
- National Key Research and Development Program of China (2015CB856302, 31770917, 2015CB553602)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- Alzheimer's disease, mitochondrial dysfunction, circulating metabolites, diagnostic biomarkers, early diagnosis, mitochondrial remodeling, metabolic reprogramming, neuroinflammation, cytokines
- MeSH terms
- Alzheimer Disease, Animals, Humans, Mitochondria, Peripheral Nervous System Diseases
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